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Application Area

Boc-D-aspartic acid α-benzyl ester

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category

BOC-Amino Acids

Catalog number

BAT-004523

CAS number

92828-64-3

Molecular Formula

C16H21NO6

Molecular Weight

323.30

IUPAC Name

(3R)-3-[(2-methylpropan-2-yl)oxycarbonylamino]-4-oxo-4-phenylmethoxybutanoic acid

Synonyms

Boc-D-Asp-Obzl; (R)-4-(BENZYLOXY)-3-((TERT-BUTOXYCARBONYL)AMINO)-4-OXOBUTANOIC ACID

Appearance

White to off-white powder

Purity

≥ 98% (HPLC)

Density

1.219 g/cm3

Melting Point

93-99 °C

Boiling Point

504.3±50.0 °C(Predicted)

Storage

Store at 2-8°C

InChI

InChI=1S/C16H21NO6/c1-16(2,3)23-15(21)17-12(9-13(18)19)14(20)22-10-11-7-5-4-6-8-11/h4-8,12H,9-10H2,1-3H3,(H,17,21)(H,18,19)/t12-/m1/s1

InChI Key

LDRWTKQWSXGSTM-GFCCVEGCSA-N

Canonical SMILES

CC(C)(C)OC(=O)NC(CC(=O)O)C(=O)OCC1=CC=CC=C1

Boc-D-aspartic acid α-benzyl ester, a protected amino acid derivative, plays a pivotal role in peptide synthesis and various biotechnological endeavors. Here are four key applications presented with high perplexity and burstiness:

Peptide Synthesis: Serving as a foundational element in peptide assembly, Boc-D-aspartic acid α-benzyl ester is a linchpin for crafting intricate peptide structures. Its Boc protecting group shields the α-amino group, streamlining the creation of elaborate peptide sequences. This compound is indispensable for generating bioactive peptides and peptide-based pharmaceuticals.

Drug Development: At the forefront of pharmaceutical exploration, Boc-D-aspartic acid α-benzyl ester acts as a catalyst for the development of peptide-based therapies. By integrating this safeguarded amino acid into peptides, researchers can fine-tune drug characteristics like stability and bioavailability. This capability empowers the formulation of targeted and potent treatments for diverse medical conditions, heralding a new era in drug design.

Protein Engineering: In the realm of protein manipulation, Boc-D-aspartic acid α-benzyl ester emerges as a key player in introducing tailored residues into protein architectures. This intervention aids in unraveling protein functionalities and crafting proteins with novel traits or enhanced attributes. Such applications are vital for forging novel enzymes, therapeutic proteins, and cutting-edge biocatalysts, propelling the frontier of protein engineering.

Bioconjugation: Leveraging the versatile ester functionality of Boc-D-aspartic acid α-benzyl ester, researchers harness its potential in bioconjugation methodologies. By linking this compound with other biomolecules, scientists engineer conjugates with augmented properties tailored for diagnostics, therapeutics, and imaging applications. This innovative approach drives the development of advanced biomedical tools and targeted delivery systems, opening avenues for precision medicine and diagnostic breakthroughs.

1. Modification of the vitamin K-dependent carboxylase assay

S Romiti, W K Kappel J Biochem Biophys Methods. 1985 May;11(1):59-68. doi: 10.1016/0165-022x(85)90041-7.

Methods are presented that describe alternative protocols for the isolation of rat liver microsomes containing the vitamin K-dependent carboxylase and the procedure in which the solubilized enzyme is assayed. The method for determining the rate of 14CO2 incorporation into low molecular weight, acid soluble substrates by the rat liver microsomal vitamin K-dependent carboxylase has been modified in order to optimize safety, accuracy and simplicity. For these studies the rat liver microsomes containing the vitamin K-dependent carboxylase were isolated by CaCl2 precipitation. These Triton X-100 solubilized microsomes were found to be equivalent to the microsomes obtained by high speed ultracentrifugation with regard to protein concentration, pentapeptide carboxylase activity, carboxylase activity, preprothrombin concentration and total carboxylatable endogenous protein substrate. This modified assay procedure requires fewer steps and pipetting transfers and is quantitatively equivalent to previously employed protocols. The described technique can be adapted for any assay where 14CO2 or H14CO3- is incorporated into non-volatile products. This newly developed assay procedure was employed to assess conditions necessary for optimal vitamin K-dependent carboxylation of the less expensive substrate, N-t-Boc-L-glutamic acid alpha-benzyl ester. The optimal conditions for the carboxylation of N-t-Boc-L-glutamic acid alpha-benzyl ester by the carboxylase were found to be 10 mM N-t-Boc-L-glutamic acid alpha-benzyl ester, 10 mM MgCl2 at 15-18 degrees C. The rate of N-t-Boc-L-glutamic acid alpha-benzyl ester carboxylation under these optimized conditions was found to be higher (1.5-fold) than the rate of carboxylation of 1 mM Phe-Leu-Glu-Glu-Ile in the presence of the cation activator, MgCl2.

2. Catalytic Asymmetric Benzylation of Azomethine Ylides Enabled by Synergistic Lewis Acid/Palladium Catalysis

Xin Chang, Jing-Di Ran, Xue-Tao Liu, Chun-Jiang Wang Org Lett. 2022 Apr 8;24(13):2573-2578. doi: 10.1021/acs.orglett.2c00865. Epub 2022 Mar 29.

The synergistic chiral Lewis acid/achiral Pd catalyst system was successfully applied in the enantioselective benzylation of various imine esters, giving a range of α-benzyl-substituted α-amino acid derivatives in satisfactory yield with excellent enantioselectivity. It is worth noting that this strategy exhibits good tolerance for bicyclic and monocyclic benzylic electrophiles. Furthermore, the utility of this synthetic protocol was demonstrated by the expedient preparation of enantioenriched antihypertensive drug α-methyl-l-dopa.

3. Catalytic asymmetric Tsuji-Trost α-benzylation reaction of N-unprotected amino acids and benzyl alcohol derivatives

Jian-Hua Liu, Wei Wen, Jian Liao, Qi-Wen Shen, Yao Lin, Zhu-Lian Wu, Tian Cai, Qi-Xiang Guo Nat Commun. 2022 May 6;13(1):2509. doi: 10.1038/s41467-022-30277-9.

Catalytic asymmetric Tsuji-Trost benzylation is a promising strategy for the preparation of chiral benzylic compounds. However, only a few such transformations with both good yields and enantioselectivities have been achieved since this reaction was first reported in 1992, and its use in current organic synthesis is restricted. In this work, we use N-unprotected amino acid esters as nucleophiles in reactions with benzyl alcohol derivatives. A ternary catalyst comprising a chiral aldehyde, a palladium species, and a Lewis acid is used to promote the reaction. Both mono- and polycyclic benzyl alcohols are excellent benzylation reagents. Various unnatural optically active α-benzyl amino acids are produced in good-to-excellent yields and with good-to-excellent enantioselectivities. This catalytic asymmetric method is used for the formal synthesis of two somatostatin mimetics and the proposed structure of natural product hypoestestatin 1. A mechanism that plausibly explains the stereoselective control is proposed.